The objective of the overall research in this laboratory is centered on achieving as complete a description as possible for the structures of peptides, proteins, nucleic acids and their complexes in solution, principally by NMR spectroscopy. At present particular emphasis is being placed on developing approaches which allow the investigation of larger and complex systems as well as increase the precision with which these solution structures can be obtained. Studies aimed at correlating structure and function, and experiments aimed at investigating protein folding are conducted. Structural studies for several proteins have been carried out. These comprise HIV-1 protease, cyanovirin-N, a hybrid thioredoxin and a replication initiator protein. In addition, work was also carried out on the folding of different quaternary states of the model protein GB1. New media for partially aligning molecules in the magnetic field were characterized and exploited for measuring residual dipolar couplings. In addition, novel NMR experiments for determining these couplings were devised.